SASDEQ7

Filamin A Ig-like domains 3-5 (FLNa3-5)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新:2019-12-06T13:07:15.624532+01:00

SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Filamin A Ig-like domains 3-5 (FLNa3-5)

浓度1.0 – 4.0 缓冲液 / pH20 mM Tris, 100 mM NaCl, 1 mM DTT / 8.0
实验温度20.0 设备 / 束线ESRF / BM29
波长0.1 nm曝光1.0 s × 10

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Filamin A Ig-like domains 3-5
查看序列
>FLNA3-5CNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAG
proteinHomo sapiensP21333478–766monomer分子数 130.76 kDa

实验曲线

曲线点数 / 列q 范围误差质量负强度点来源文件
11037[3]0.060004–4.93699 1/nm含误差列缺失 02sasbdb/entries/q7/sasdeq7/source/SASDEQ7.dat
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2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)7.340.5nm
i0Guinier25.640.1arbitrary
i0P(r)25.64—arbitrary
mwExperimental24.7—kDa
porod_volumePorod39.0—nm³
rgGuinier2.190.1nm
rgP(r)2.2—nm

这些数值是 SASBDB 来源记录,不是 SAXSdb 对实验曲线重新计算的结果。

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3. 来源拟合与模型 Source Fits & Models

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4. 来源文件索引 Source Files

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5. 实验说明与论文 Experiment & Publication

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6. 完整来源记录 Complete Source Record

下列内容直接来自 SASBDB 条目。字段没有值时显示“—”;未声明的单位不会由 SAXSdb 猜测。

打开 SASBDB 原始条目

缓冲液与样品属性

缓冲液名称20 mM Tris, 100 mM NaCl, 1 mM DTT缓冲液浓度—
pH8.0添加剂—
缓冲液说明—
纯度测定方法—消光系数—
吸收值—散射对比度—
比体积 / 干体积— / —混合物 / 氘代— / —

采集条件与仪器

测量日期2017-02-10储存 / 测量温度— / 20.0
曝光时间1.0帧数10
波长0.1样品-探测器距离2.9
光源X-ray synchrotron探测器Pilatus 1M
机构 / 束线ESRF / BM29 · Grenoble, France
q 范围0.06 – 4.937样品体积 / 流速— / —

SASBDB 原始图

实验 I(q)
实验 I(q)
实验 I(q) log-log
实验 I(q) log-log
Guinier 图
Guinier 图
Kratky 图
Kratky 图
P(r) 图
P(r) 图

可下载文件

类别文件状态大小校验值下载与查看
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curve:来源记录
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pddf:来源记录
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全部来源字段(无筛选)

这里自动展开来源记录中的每一个字段,包括空值、列表成员和页面上方已展示过的字段。

summary.json:159 个字段值
字段路径原始值
codeSASDEQ7
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleNon-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.
project.publication.titleNon-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.
project.publication.author_listHaataja TJK, Bernardi RC, Lecointe S, Capoulade R, Merot J, Pentikäinen U
project.publication.journalStructure
project.publication.doi10.1016/j.str.2018.09.007
project.publication.pmid30344108
project.publication.published_date2018 Oct 9
project.statusreleased
project.submitted_date2018-11-12
project.released_date2018-11-12
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sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDEQ7.sascif
experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameFilamin A Ig-like domains 3-5
experiment.sample.molecule[0].short_nameFLNa3-5
experiment.sample.molecule[0].sequence>FLNa3-5 CNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeP21333
experiment.sample.molecule[0].uniprot_range_first478
experiment.sample.molecule[0].uniprot_range_last766
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV SKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK LVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKL PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQ VITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKK RAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLF AGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVI QDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNP SACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGF EYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVE AIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFM ADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVE ALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVA KTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTP RGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAK AAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSP FSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKV EPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGG SAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILF ADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSE AGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQC YGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVE YTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVET RGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKV PVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVV DNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGV PASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILI KYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAG KGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTA LAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIK KGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYV DYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTC SVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDL SLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVIS QSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDG TCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHC DLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQH VPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSK AEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSL QESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVY LIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAG ALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPR LVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTV DCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGS PYRVVVP
experiment.sample.molecule[0].mw30.76
experiment.sample.molecule[0].total_mw30.76
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name20 mM Tris, 100 mM NaCl, 1 mM DTT
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameFilamin A Ig-like domains 3-5 (FLNa3-5)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressJyväskylän, Finland
experiment.contributor[0].affiliation[0].full_nameUniversity of Jyväskylä
experiment.contributor[0].affiliation[0].webpagehttps://www.jyu.fi
experiment.contributor[0].contributor_nameTatu
experiment.contributor[0].contributor_surnameHaataja
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2017-02-10
experiment.storage_temperaturenull
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.1
experiment.sample_detector_distance2.9
experiment.concentration_min1.0
experiment.concentration_max4.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.06
experiment.s_max4.937
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwarePDB (Protein Data Bank)
fits[0].models[0].pdb_link[0].pdb_code4m9p
fits[0].models[0].pdb_link[0].ext_code4M9P
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fits[0].models[0].type_of_modelatomic
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fits[0].models[0].model_mw30.74
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fits[0].models[0].user251
fits[0].fit_unit1/A
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fits[0].softwareCRYSOL
fits[0].chi_square_value1.001
fits[0].p_value0.0
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fits[0].description
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version4.6
i0_calibration_standardnull
descriptionSAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated fragment (SASDEP7).
experiment_descriptionSynchrotron SAXS data from solutions of Filamin A Ig-like domains 3-5 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 20°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unitarbitrary
experimental_mw24.7
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i025.64
pddf_i0_errornull
guinier_i025.64
guinier_i0_error0.1
pddf_rg2.2
pddf_rg_errornull
guinier_rg2.19
guinier_rg_error0.1
pddf_dmax7.34
pddf_dmax_error0.5
porod_volume39.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first8
guinier_point_last114
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDEQ7_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDEQ7
statussuccess
started_at2026-08-11T16:27:12.174165+00:00
finished_at2026-08-11T16:27:20.697810+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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files[4].rolefull_entry_zip
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查看完整 summary.json 原文
{
  "code": "SASDEQ7",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.",
    "publication": {
      "title": "Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A.",
      "author_list": "Haataja TJK, Bernardi RC, Lecointe S, Capoulade R, Merot J, Pentikäinen U",
      "journal": "Structure",
      "doi": "10.1016/j.str.2018.09.007",
      "pmid": "30344108",
      "published_date": "2018 Oct 9"
    },
    "status": "released",
    "submitted_date": "2018-11-12",
    "released_date": "2018-11-12"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDEQ7.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDEQ7.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ7_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ7_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDEQ7_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ7_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDEQ7.sascif",
  "experiment": {
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        "name": "Pilatus 1M",
        "resolution": 172.0
      },
      "name": "ESRF",
      "city": "Grenoble",
      "country": "France",
      "beamline_name": "BM29",
      "beam_geometry": "",
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
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          "long_name": "Filamin A Ig-like domains 3-5",
          "short_name": "FLNa3-5",
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          "organism": "Homo sapiens",
          "uniprot_code": "P21333",
          "uniprot_range_first": 478,
          "uniprot_range_last": 766,
          "oligomerization": "monomer",
          "molecular_type": "protein",
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          "total_mw": 30.76,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "20 mM Tris, 100 mM NaCl, 1 mM DTT",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Filamin A Ig-like domains 3-5 (FLNa3-5)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Jyväskylän, Finland",
            "full_name": "University of Jyväskylä",
            "webpage": "https://www.jyu.fi"
          }
        ],
        "contributor_name": "Tatu",
        "contributor_surname": "Haataja",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2017-02-10",
    "storage_temperature": null,
    "cell_temperature": 20.0,
    "exposure_time": 1.0,
    "number_of_frames": 10,
    "wavelength": 0.1,
    "sample_detector_distance": 2.9,
    "concentration_min": 1.0,
    "concentration_max": 4.0,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.06,
    "s_max": 4.937,
    "total_exposure_time": null,
    "seccolumn": null
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        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDEQ7_fit1_model1_img.png",
          "software": "PDB (Protein Data Bank)",
          "pdb_link": [
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              "pdb_code": "4m9p",
              "ext_code": "4M9P",
              "ext_type": "pdb",
              "difference_with_model": "identical"
            }
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          "model_title": null,
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          "software_version": null,
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          "model_mw": 30.74,
          "bead_radius": null,
          "log": null,
          "symmetry": null,
          "comment": null,
          "user": 251
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      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/FLNa35_crysol_fit_img.png",
      "software": "CRYSOL",
      "chi_square_value": 1.001,
      "p_value": 0.0,
      "fit_residual_plot": "fit4columns1920_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDEQ7_fit1.fit",
      "fit_log": null,
      "software_version": null,
      "description": ""
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  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "4.6",
  "i0_calibration_standard": null,
  "description": "SAXS data describing the Filamin A Ig-like domains 3-5 in solution. The experiment was done to enable comparison with the corresponding P637Q mutated  fragment (SASDEP7).",
  "experiment_description": "Synchrotron SAXS data from solutions of Filamin A Ig-like domains 3-5 in 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 20°C. 10 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.",
  "tags": [],
  "intensity_unit": "arbitrary",
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  "experimental_mw_error": null,
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  "guinier_rg_error": 0.1,
  "pddf_dmax": 7.34,
  "pddf_dmax_error": 0.5,
  "porod_volume": 39.0,
  "porod_volume_error": null,
  "estimated_volume": null,
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  "guinier_point_first": 8,
  "guinier_point_last": 114,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDEQ7_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
{
  "code": "SASDEQ7",
  "status": "success",
  "started_at": "2026-08-11T16:27:12.174165+00:00",
  "finished_at": "2026-08-11T16:27:20.697810+00:00",
  "source_last_modified": "2019-12-06T13:07:15.624532+01:00",
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